Structure of PDB 3amm Chain B

Receptor sequence
>3ammB (length=261) Species: 2336 (Thermotoga maritima) [Search protein sequence]
HHHHMVLMTKPGTSDFVWNGIPLSMELNLWNIKEYSGSVAMKFDGEKITF
DADIQNLSPKEPERYVLGYPEFYYGYKPWENHTAEGSKLPVPVSSMKSFS
VEVSFDIHHEPSLPLNFAMETWLTREKYQTEASIGDVEIMVWFYFNNLTP
GGEKIEEFTIPFVLNGESVEGTWELWLAEWGWDYLAFRLKDPVKKGRVKF
DVRHFLDAAGKALSSSARVKDFEDLYFTVWEIGTEFGSPETKSAQFGWKF
ENFSIDLEVRE
3D structure
PDB3amm Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima
ChainB
Resolution1.98 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.2.1.4: cellulase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 BGC B Y61 T145 G147 Y65 T149 G151
BS02 BGC B R60 W138 W176 Y180 E231 R64 W142 W180 Y184 E235
BS03 BGC B W26 R60 Y65 E134 E231 W30 R64 Y69 E138 E235
BS04 BGC B W26 K73 W75 W30 K77 W79
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0000272 polysaccharide catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3amm, PDBe:3amm, PDBj:3amm
PDBsum3amm
PubMed21268113
UniProtQ60032

[Back to BioLiP]